2008
DOI: 10.1271/bbb.80410
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Asymmetric Synthesis of (S)-α-Methylbenzylamine by RecombinantEscherichia coliCo-Expressing Omega-Transaminase and Acetolactate Synthase

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Cited by 53 publications
(32 citation statements)
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“…[21] For this purpose, several types of enzymes have already been applied such as lactate dehydrogenase, [13,22] alanine dehydrogenase, [12,23] pyruvate decarboxylase [24] and acetolactate synthase. [25] In this study, commercial lactate dehydrogenase from rabbit muscle (LDH system) and l-alanine dehydroge-nase from Bacillus subtilis [26] (AlaDH system) were employed (Scheme 1). The latter enzyme was overexpressed in E. coli with a His 6 -tag and used as purified enzyme.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…[21] For this purpose, several types of enzymes have already been applied such as lactate dehydrogenase, [13,22] alanine dehydrogenase, [12,23] pyruvate decarboxylase [24] and acetolactate synthase. [25] In this study, commercial lactate dehydrogenase from rabbit muscle (LDH system) and l-alanine dehydroge-nase from Bacillus subtilis [26] (AlaDH system) were employed (Scheme 1). The latter enzyme was overexpressed in E. coli with a His 6 -tag and used as purified enzyme.…”
Section: Resultsmentioning
confidence: 99%
“…The ω-TA from Vibrio fluvialis (VF-ωTA) has been investigated previously, and comprehensive data for initial reaction rates are available for various substrates, [21,27] which employ the enzyme as a whole-cell catalyst in aqueous and biphasic systems [28] and immobilized enzymes. [29] Additionally, the applicability of VF-ωTA has been evaluated on a pilot-plant scale with a membrane reactor [30] and a packedbed reactor.…”
Section: Resultsmentioning
confidence: 99%
“…Several authors (Cassimjee et al, 2010;Fotheringham et al, 1999;Koszelewski et al, 2010b;Panke et al, 1999;Yun and Kim, 2008) have shown that chromosomal integration of genes under a suitable regulatory system to an E. coli or P. pastoris mutant is a very useful route for constructing a whole-cell biocatalyst that is able to synthesize chiral amines to high specific activities and that can maintain activity for extended periods under reaction conditions in the presence of an organic phase. However, the adequate expression level of each protein still remains a challenge (Kratzer et al, 2010).…”
Section: Whole-cell Biocatalysismentioning
confidence: 99%
“…The kinetic resolution of various amines by ω-TA have been typically carried out using pyruvate as an amino acceptor to accept the amino group from the amine, which is the main target compound [9][10][11][12][13][14][15][16]. However, in this study F-pyruvate was used as a target substrate and (S)-α-MBA was used as a co-substrate to donate the amino group to Fpyruvate.…”
Section: Substrate and Product Inhibition Of ω-Ta For Asymmetric Syntmentioning
confidence: 99%
“…In addition, this reaction does not require external cofactor regeneration [9]. TAs belonging to subgroup III are called ω-TAs, and include ω-amino acid:pyruvate TA, ornithine TA, 4-aminobutyrate TA, and others [10]. Unlike α-TA, ω-TA can transfer an amino group from a non-α position amino acid (such as 4-aminobutyrate) or an amine compound with no carboxylic group (such as α-MBA) to an amino acceptor (such as 2-ketoglutarate or pyruvate) [10,11].…”
Section: Introductionmentioning
confidence: 99%